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Volumn 137, Issue 7, 1997, Pages 1663-1681

Cross talk between adhesion molecules: Control of N-cadherin activity by intracellular signals elicited by β1 and β3 integrins in migrating neural crest cells

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; CELL ADHESION MOLECULE; FIBRONECTIN; INTEGRIN;

EID: 0031002437     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.7.1663     Document Type: Article
Times cited : (144)

References (112)
  • 1
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • Adams, C.L., W.J. Nelson, and S.J. Smith. 1996. Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J. Cell Biol. 135:1899-1911.
    • (1996) J. Cell Biol. , vol.135 , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 2
    • 0026699349 scopus 로고
    • Expression of cell adhesion molecules during initiation of and cessation of neural crest cell migration
    • Akitaya, T., and M. Bronner-Fraser. 1992. Expression of cell adhesion molecules during initiation of and cessation of neural crest cell migration. Dev. Dyn. 194:12-20.
    • (1992) Dev. Dyn. , vol.194 , pp. 12-20
    • Akitaya, T.1    Bronner-Fraser, M.2
  • 3
    • 0022367152 scopus 로고
    • The interaction of fibronectin fragments with fibroblastic cells
    • Akiyama, S.K., E. Hasegawa, T. Hasegawa, and K.M. Yamada. 1985. The interaction of fibronectin fragments with fibroblastic cells. J. Biol. Chem. 260:13256-13260.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13256-13260
    • Akiyama, S.K.1    Hasegawa, E.2    Hasegawa, T.3    Yamada, K.M.4
  • 4
    • 0024383791 scopus 로고
    • Dissecting tumor cell invasion: Epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell-cell adhesion
    • Behrens, J., M.M. Mareel, F.M. Van Roy, and W. Birchmeier. 1989. Dissecting tumor cell invasion: epithelial cells acquire invasive properties after the loss of uvomorulin-mediated cell-cell adhesion. J. Cell Biol. 108:2435-2447.
    • (1989) J. Cell Biol. , vol.108 , pp. 2435-2447
    • Behrens, J.1    Mareel, M.M.2    Van Roy, F.M.3    Birchmeier, W.4
  • 5
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene
    • Behrens, J., L. Vakaet, R. Friis, E. Winterhager, F. Van Roy, M.M. Mareel, and W. Birchmeier. 1993. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J. Cell Biol. 120:757-766.
    • (1993) J. Cell Biol. , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 6
    • 0028171951 scopus 로고
    • Integrin αvβ3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor α5β1
    • Blystone, S.D., I.L. Graham, F.P. Lindberg, and E.J. Brown. 1994. Integrin αvβ3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor α5β1. J. Cell Biol. 127:1129-1137.
    • (1994) J. Cell Biol. , vol.127 , pp. 1129-1137
    • Blystone, S.D.1    Graham, I.L.2    Lindberg, F.P.3    Brown, E.J.4
  • 7
    • 0028983057 scopus 로고
    • Integrin β3 cytoplasmic tail is necessary and sufficient for regulation of α5β1 phagocytosis by αvβ3 and integrin-associated protein
    • Blystone, S.D., F.P. Lindberg, S.E. LaFlamme, and E.J. Brown. 1995. Integrin β3 cytoplasmic tail is necessary and sufficient for regulation of α5β1 phagocytosis by αvβ3 and integrin-associated protein. J. Cell Biol. 130:745-754.
    • (1995) J. Cell Biol. , vol.130 , pp. 745-754
    • Blystone, S.D.1    Lindberg, F.P.2    LaFlamme, S.E.3    Brown, E.J.4
  • 8
    • 0021720476 scopus 로고
    • Biological active synthetic peptides as probes of embryonic development: A competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos
    • Boucaut, J.-C., T. Darribère, T.J. Poole, H. Aoyama, K.M. Yamada, and J.P. Thiery. 1984. Biological active synthetic peptides as probes of embryonic development: a competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos. J. Cell Biol. 99:1822-1830.
    • (1984) J. Cell Biol. , vol.99 , pp. 1822-1830
    • Boucaut, J.-C.1    Darribère, T.2    Poole, T.J.3    Aoyama, H.4    Yamada, K.M.5    Thiery, J.P.6
  • 10
    • 0021997189 scopus 로고
    • Alteration in neural crest migration by a monoclonal antibody that affects cell adhesion
    • Bronner-Fraser, M. 1985. Alteration in neural crest migration by a monoclonal antibody that affects cell adhesion. J. Cell Biol. 101:610-617.
    • (1985) J. Cell Biol. , vol.101 , pp. 610-617
    • Bronner-Fraser, M.1
  • 11
    • 0022993632 scopus 로고
    • An antibody to a receptor for fibronectin and laminin perturbs cranial neural crest development in vivo
    • Bronner-Fraser, M. 1986. An antibody to a receptor for fibronectin and laminin perturbs cranial neural crest development in vivo. Dev. Biol. 117:528-536.
    • (1986) Dev. Biol. , vol.117 , pp. 528-536
    • Bronner-Fraser, M.1
  • 12
    • 0027359537 scopus 로고
    • Neural crest cell migration in the developing embryo
    • Bronner-Fraser, M. 1993. Neural crest cell migration in the developing embryo. Trends Cell Biol. 3:392-397.
    • (1993) Trends Cell Biol. , vol.3 , pp. 392-397
    • Bronner-Fraser, M.1
  • 13
    • 0026698879 scopus 로고
    • Effects of antibodies against N-cadherin and N-CAM on the cranial neural crest and neural tube
    • Bronner-Fraser, M., J.J. Wolf, and B.A. Murray. 1992. Effects of antibodies against N-cadherin and N-CAM on the cranial neural crest and neural tube. Dev. Biol. 153:291-301.
    • (1992) Dev. Biol. , vol.153 , pp. 291-301
    • Bronner-Fraser, M.1    Wolf, J.J.2    Murray, B.A.3
  • 14
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • Brooks, P.C., R.A.F. Clark, and D.A. Cheresh. 1994. Requirement of vascular integrin αvβ3 for angiogenesis. Science (Wash. DC). 264:569-571.
    • (1994) Science (Wash. DC) , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.F.2    Cheresh, D.A.3
  • 15
    • 0025666501 scopus 로고
    • Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins
    • Brown, E., L. Hooper, T. Ho, and H. Gresham. 1990. Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins. J. Cell Biol. 111:2785-2794.
    • (1990) J. Cell Biol. , vol.111 , pp. 2785-2794
    • Brown, E.1    Hooper, L.2    Ho, T.3    Gresham, H.4
  • 16
    • 0026596337 scopus 로고
    • Distinct cellular functions mediated by different VLa integrin a subunit cytoplasmic domains
    • Chan, B.M.C., P.D. Kassner, J.A. Schiro, H.R. Byers, T.S. Kupper, and M.E. Hemler. 1992. Distinct cellular functions mediated by different VLA integrin a subunit cytoplasmic domains. Cell. 68:1051-1060.
    • (1992) Cell , vol.68 , pp. 1051-1060
    • Chan, B.M.C.1    Kassner, P.D.2    Schiro, J.A.3    Byers, H.R.4    Kupper, T.S.5    Hemler, M.E.6
  • 17
    • 0021946006 scopus 로고
    • Development of cell surface linkage complexes in cultured fibroblasts
    • Chen, W.-T., E. Hasegawa, T. Hasegawa, C. Weinstock, and K.M. Yamada. 1985. Development of cell surface linkage complexes in cultured fibroblasts. J. Cell Biol. 100:1103-1114.
    • (1985) J. Cell Biol. , vol.100 , pp. 1103-1114
    • Chen, W.-T.1    Hasegawa, E.2    Hasegawa, T.3    Weinstock, C.4    Yamada, K.M.5
  • 18
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and J.S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science (Wash. DC). 268:233-268.
    • (1995) Science (Wash. DC) , vol.268 , pp. 233-268
    • Clark, E.A.1    Brugge, J.S.2
  • 19
    • 0026706420 scopus 로고
    • Transforming growth factor-β control of cell-substratum adhesion during avian neural crest cell emigration in vitro
    • Delannet, M., and J.-L. Duband. 1992. Transforming growth factor-β control of cell-substratum adhesion during avian neural crest cell emigration in vitro. Development (Camb.). 116:275-287.
    • (1992) Development (Camb.) , vol.116 , pp. 275-287
    • Delannet, M.1    Duband, J.-L.2
  • 20
    • 0028170046 scopus 로고
    • Specific roles of the αVβ1, αVβ3 and αVβ5 integrins in avian neural crest cell adhesion and migration on vitronectin
    • Delannet, M., F. Martin, B. Bossy, D.A. Cheresh, L.F. Reichardt, and J.-L. Duband. 1994. Specific roles of the αVβ1, αVβ3 and αVβ5 integrins in avian neural crest cell adhesion and migration on vitronectin. Development (Camb.). 120:2687-2702.
    • (1994) Development (Camb.) , vol.120 , pp. 2687-2702
    • Delannet, M.1    Martin, F.2    Bossy, B.3    Cheresh, D.A.4    Reichardt, L.F.5    Duband, J.-L.6
  • 21
    • 0022619534 scopus 로고
    • Cell adhesion and migration in the early vertebrate embryo: Location and possible role of the putative fibronectin-receptor complex
    • Duband, J.-L., S. Rocher, W.-T. Chen, K.M. Yamada, and J.P. Thiery. 1986. Cell adhesion and migration in the early vertebrate embryo: location and possible role of the putative fibronectin-receptor complex. J. Cell Biol. 102:160-178.
    • (1986) J. Cell Biol. , vol.102 , pp. 160-178
    • Duband, J.-L.1    Rocher, S.2    Chen, W.-T.3    Yamada, K.M.4    Thiery, J.P.5
  • 22
    • 0024095296 scopus 로고
    • The fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells
    • Duband, J.-L., G.H. Nuckolls, A. Ishihara, T. Hasegawa, K.M. Yamada, J.P. Thiery, and K. Jacobson. 1988. The fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells. J. Cell Biol. 107: 1385-1396.
    • (1988) J. Cell Biol. , vol.107 , pp. 1385-1396
    • Duband, J.-L.1    Nuckolls, G.H.2    Ishihara, A.3    Hasegawa, T.4    Yamada, K.M.5    Thiery, J.P.6    Jacobson, K.7
  • 23
    • 0023934829 scopus 로고
    • Spatial and temporal distribution of the adherens-junction-associated adhesion molecule A-CAM during avian embryogenesis
    • Duband, J.-L., T. Volberg, I. Sabanay, J.P. Thiery, and B. Geiger. 1988. Spatial and temporal distribution of the adherens-junction-associated adhesion molecule A-CAM during avian embryogenesis. Development (Camb.). 103:325-344.
    • (1988) Development (Camb.) , vol.103 , pp. 325-344
    • Duband, J.-L.1    Volberg, T.2    Sabanay, I.3    Thiery, J.P.4    Geiger, B.5
  • 24
    • 0025827797 scopus 로고
    • Neural crest cell locomotion induced by antibodies to β1 integrins: A tool for studying the roles of substratum molecular avidity and density in migration
    • Duband, J.-L., S. Dufour, S.S. Yamada, K.M. Yamada, and J.P. Thiery. 1991. Neural crest cell locomotion induced by antibodies to β1 integrins: a tool for studying the roles of substratum molecular avidity and density in migration. J. Cell Sci. 98:517-532.
    • (1991) J. Cell Sci. , vol.98 , pp. 517-532
    • Duband, J.-L.1    Dufour, S.2    Yamada, S.S.3    Yamada, K.M.4    Thiery, J.P.5
  • 25
    • 0000154372 scopus 로고
    • Neural crest cells: Strategies to generate lineage diversification in vitro
    • J. Cohen and G.P. Wilkin, editors. Oxford University Press, Oxford, UK
    • Duband, J.-L., M. Delannet, and F. Monier-Gavelle. 1995. Neural crest cells: strategies to generate lineage diversification in vitro. In Neural Cell Culture: A Practical Approach. J. Cohen and G.P. Wilkin, editors. Oxford University Press, Oxford, UK. 133-152.
    • (1995) Neural Cell Culture: A Practical Approach , pp. 133-152
    • Duband, J.-L.1    Delannet, M.2    Monier-Gavelle, F.3
  • 26
    • 84939403755 scopus 로고
    • Epithelium-mesenchyme transition during neural crest development
    • Duband, J.-L., F. Monier, M. Delannet, and D.F. Newgreen. 1995. Epithelium-mesenchyme transition during neural crest development. Acta Anat. 154:63-78.
    • (1995) Acta Anat. , vol.154 , pp. 63-78
    • Duband, J.-L.1    Monier, F.2    Delannet, M.3    Newgreen, D.F.4
  • 27
    • 0024075252 scopus 로고
    • Attachment, spreading, and locomotion of avian neural crest cells are mediated by multiple adhesion sites on fibronectin molecules
    • Dufour, S., J.-L. Duband, M.J. Humphries, M. Obara, K.M. Yamada, and J.P. Thiery. 1988. Attachment, spreading, and locomotion of avian neural crest cells are mediated by multiple adhesion sites on fibronectin molecules. EMBO (Eur. Mol. Biol. Organ.) J. 7:2661-2671.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 2661-2671
    • Dufour, S.1    Duband, J.-L.2    Humphries, M.J.3    Obara, M.4    Yamada, K.M.5    Thiery, J.P.6
  • 28
    • 0027439963 scopus 로고
    • The role of cell-cell and cell-matrix interactions in the morphogenesis of the neural crest
    • Erickson, C.A., and R. Perris. 1993. The role of cell-cell and cell-matrix interactions in the morphogenesis of the neural crest. Dev. Biol. 159:60-74.
    • (1993) Dev. Biol. , vol.159 , pp. 60-74
    • Erickson, C.A.1    Perris, R.2
  • 29
    • 0029094471 scopus 로고
    • Cadherin transfection of Xenopus XTC cells downregulates expression of substrate-adhesion molecules
    • Finnemann, S., M. Külh. G. Otto, and D. Wedlich. 1995. Cadherin transfection of Xenopus XTC cells downregulates expression of substrate-adhesion molecules. Mol. Cell. Biol. 15:5082-5091.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5082-5091
    • Finnemann, S.1    Külh, M.2    Otto, G.3    Wedlich, D.4
  • 32
    • 0020393662 scopus 로고
    • 2+-transport ATPase and brain phosphodiesterase by activators and inhibitors
    • 2+-transport ATPase and brain phosphodiesterase by activators and inhibitors. Biochem. J. 207:541-548.
    • (1982) Biochem. J. , vol.207 , pp. 541-548
    • Gietzen, K.1    Sadorf, I.2    Bader, H.3
  • 33
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B.M. 1996. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell. 84:345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 34
    • 0025077629 scopus 로고
    • Bifunctional role of glycosphingolipid: Modulators for transmembrane signaling and mediators for cellular interactions
    • Hakomori, S. 1990. Bifunctional role of glycosphingolipid: modulators for transmembrane signaling and mediators for cellular interactions. J. Biol. Chem. 265:18713-18716.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18713-18716
    • Hakomori, S.1
  • 36
    • 0022621979 scopus 로고
    • Expression of N-cadherin adhesion molecules associated with early morphogenetic events in chick development
    • Hatta, K., and M. Takeichi. 1986. Expression of N-cadherin adhesion molecules associated with early morphogenetic events in chick development. Nature (Lond.). 320:447-449.
    • (1986) Nature (Lond.) , vol.320 , pp. 447-449
    • Hatta, K.1    Takeichi, M.2
  • 37
    • 0023117283 scopus 로고
    • Spatial and temporal expression pattern of N-cadherin cell adhesion molecules correlated with morphogenetic processes of chicken embryos
    • Hatta, K., S. Takagi, H. Fujisawa, and M. Takeichi. 1987. Spatial and temporal expression pattern of N-cadherin cell adhesion molecules correlated with morphogenetic processes of chicken embryos. Dev. Biol. 120: 215-227.
    • (1987) Dev. Biol. , vol.120 , pp. 215-227
    • Hatta, K.1    Takagi, S.2    Fujisawa, H.3    Takeichi, M.4
  • 39
    • 0026498038 scopus 로고
    • Inhibition of neutrophil chemokinesis on vitronectin by inhibitors of calcineurin
    • Hendey, B., C.B. Klee, and F.R. Maxfield. 1992. Inhibition of neutrophil chemokinesis on vitronectin by inhibitors of calcineurin. Science (Wash. DC). 258:296-299.
    • (1992) Science (Wash. DC) , vol.258 , pp. 296-299
    • Hendey, B.1    Klee, C.B.2    Maxfield, F.R.3
  • 41
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex assembly
    • Hinck, L., I. Näthke, J. Papkoff, and W.J. Nelson. 1994. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell Biol. 125:1327-1340.
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Näthke, I.2    Papkoff, J.3    Nelson, W.J.4
  • 42
    • 0028258445 scopus 로고
    • Wnt-1 modulates cell-cell adhesion in mammalian cells by stabilizing β-catenin binding to the cell adhesion protein cadherin
    • Hinck, L., W.J. Nelson, and J. Papkoff. 1994. Wnt-1 modulates cell-cell adhesion in mammalian cells by stabilizing β-catenin binding to the cell adhesion protein cadherin. J. Cell Biol. 124:729-741.
    • (1994) J. Cell Biol. , vol.124 , pp. 729-741
    • Hinck, L.1    Nelson, W.J.2    Papkoff, J.3
  • 43
    • 0027957163 scopus 로고
    • Evidence that cadherins play a role in the downregulation of integrin expression that occurs during keratinocyte terminal differentiation
    • Hodivala, K.J., and F.M. Watt. 1994. Evidence that cadherins play a role in the downregulation of integrin expression that occurs during keratinocyte terminal differentiation. J. Cell Biol. 124:589-600.
    • (1994) J. Cell Biol. , vol.124 , pp. 589-600
    • Hodivala, K.J.1    Watt, F.M.2
  • 44
    • 0022342663 scopus 로고
    • The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin
    • Horwitz, A., K. Duggan, R. Greggs, C. Decker, and C. Buck. 1985. The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin. J. Cell Biol. 101:2134-2144.
    • (1985) J. Cell Biol. , vol.101 , pp. 2134-2144
    • Horwitz, A.1    Duggan, K.2    Greggs, R.3    Decker, C.4    Buck, C.5
  • 45
    • 0028170977 scopus 로고
    • β-Catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
    • Hoschuetzky, H., H. Aberle, and R. Kemler. 1994. β-Catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J. Cell Biol. 127:1375-1380.
    • (1994) J. Cell Biol. , vol.127 , pp. 1375-1380
    • Hoschuetzky, H.1    Aberle, H.2    Kemler, R.3
  • 46
    • 0026503656 scopus 로고
    • Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons
    • Hynes, R.O., and A.D. Lander. 1992. Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons. Cell. 68: 303-322.
    • (1992) Cell , vol.68 , pp. 303-322
    • Hynes, R.O.1    Lander, A.D.2
  • 49
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
    • Kinch, M.S., G.J. Clark., C.J. Der, and K. Burridge. 1995. Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. J. Cell Biol. 130:461-471.
    • (1995) J. Cell Biol. , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.J.2    Der, C.J.3    Burridge, K.4
  • 50
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 51
    • 0028043735 scopus 로고
    • Receptor tyrosine kinase signaling required for integrin αvβ5 directed cell motility but not adhesion on vitronectin
    • Klemke, R.L., M. Yebra, E.M. Bayna, and D.A. Cheresh. 1994. Receptor tyrosine kinase signaling required for integrin αvβ5 directed cell motility but not adhesion on vitronectin. J. Cell Biol. 127:859-866.
    • (1994) J. Cell Biol. , vol.127 , pp. 859-866
    • Klemke, R.L.1    Yebra, M.2    Bayna, E.M.3    Cheresh, D.A.4
  • 52
    • 0029973887 scopus 로고    scopus 로고
    • Integrin-dependent signal transduction
    • Lafrenie, R.M., and K.M. Yamada. 1996. Integrin-dependent signal transduction. J. Cell. Biochem. 61:543-553.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 543-553
    • Lafrenie, R.M.1    Yamada, K.M.2
  • 53
    • 0028204058 scopus 로고
    • Neural crest cell interactions with laminin: Structural requirements and localization of the binding site for α1β1 integrin
    • Lallier, T., R. Deutzmann, R. Perris, and M. Bronner-Fraser. 1994. Neural crest cell interactions with laminin: structural requirements and localization of the binding site for α1β1 integrin. Develop. Biol. 162:451-464.
    • (1994) Develop. Biol. , vol.162 , pp. 451-464
    • Lallier, T.1    Deutzmann, R.2    Perris, R.3    Bronner-Fraser, M.4
  • 54
    • 0023470509 scopus 로고
    • Synthetic peptides that mimic the adhesive recognition signal of fibronectin: Differential effects on cell-cell and cell-substratum adhesion in embryonic chick cells
    • Lash, J.W., K.K. Linask, and K.M. Yamada. 1987. Synthetic peptides that mimic the adhesive recognition signal of fibronectin: differential effects on cell-cell and cell-substratum adhesion in embryonic chick cells. Dev. Biol. 123:411-420.
    • (1987) Dev. Biol. , vol.123 , pp. 411-420
    • Lash, J.W.1    Linask, K.K.2    Yamada, K.M.3
  • 55
    • 0028978448 scopus 로고
    • 2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils
    • 2+- and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils. Nature (Lond.). 377:75-79.
    • (1995) Nature (Lond.) , vol.377 , pp. 75-79
    • Lawson, M.A.1    Maxfield, F.R.2
  • 56
    • 0004007167 scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Le Douarin, N.M. 1982. The Neural Crest. Cambridge University Press, Cambridge, UK.
    • (1982) The Neural Crest
    • Le Douarin, N.M.1
  • 57
    • 0027513593 scopus 로고
    • Integrin β1- and β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms
    • Leavesley, D.I., M.A. Schwartz, M. Rosenfeld, and D.A. Cheresh. 1993. Integrin β1- and β3-mediated endothelial cell migration is triggered through distinct signaling mechanisms. J. Cell Biol. 121:163-170.
    • (1993) J. Cell Biol. , vol.121 , pp. 163-170
    • Leavesley, D.I.1    Schwartz, M.A.2    Rosenfeld, M.3    Cheresh, D.A.4
  • 58
    • 0025678297 scopus 로고
    • Modes of cell migration in the vertebrate embryo
    • Levi, G., J.-L. Duband, and J.P. Thiery. 1990. Modes of cell migration in the vertebrate embryo. Int. Rev. Cytol. 123:201-252.
    • (1990) Int. Rev. Cytol. , vol.123 , pp. 201-252
    • Levi, G.1    Duband, J.-L.2    Thiery, J.P.3
  • 59
    • 0028173015 scopus 로고
    • The pathophysiologic role of α4 integrins in vivo
    • Lobb, R.R., and M.E. Hemler. 1994. The pathophysiologic role of α4 integrins in vivo. J. Clin. Invest. 94:1722-1728.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1722-1728
    • Lobb, R.R.1    Hemler, M.E.2
  • 60
    • 0029858914 scopus 로고    scopus 로고
    • Integrin engagement mediates tyrosine phosphorylation on platelet-endothelial cell adhesion molecule 1
    • Lu, T.T., L.G. Yan, and J.A. Madri. 1996. Integrin engagement mediates tyrosine phosphorylation on platelet-endothelial cell adhesion molecule 1. Proc. Natl. Acad. Sci. USA. 93:11808-11813.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11808-11813
    • Lu, T.T.1    Yan, L.G.2    Madri, J.A.3
  • 61
    • 0024385914 scopus 로고
    • Tyrphostins inhibit epidermal growth factor (EGF)-receptor tyrosine kinase activity in living cells and EGF-stimulated cell proliferation
    • Lyall, R.M., A. Zilberstein, A. Gazit, C. Gilon, A. Levitzki, and J. Schlessinger. 1989. Tyrphostins inhibit epidermal growth factor (EGF)-receptor tyrosine kinase activity in living cells and EGF-stimulated cell proliferation. J. Biol. Chem. 264:14503-14509.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14503-14509
    • Lyall, R.M.1    Zilberstein, A.2    Gazit, A.3    Gilon, C.4    Levitzki, A.5    Schlessinger, J.6
  • 62
    • 0026629850 scopus 로고
    • The dermal-epidermal junction of human skin contains a novel laminin variant
    • Marinkovich, M.P., G.P. Lunstrum, D.R. Keene, and R.E. Burgeson. 1992. The dermal-epidermal junction of human skin contains a novel laminin variant. J. Cell Biol. 119:695-703.
    • (1992) J. Cell Biol. , vol.119 , pp. 695-703
    • Marinkovich, M.P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 63
    • 0026083945 scopus 로고
    • Attachment to fibronectin or vitronectin makes human neutrophil migration sensitive to alterations in cytosolic free calcium concentration
    • Marks, P.W., B. Hendey, and F.R. Maxfield. 1991. Attachment to fibronectin or vitronectin makes human neutrophil migration sensitive to alterations in cytosolic free calcium concentration. J. Cell Biol. 112:149-158.
    • (1991) J. Cell Biol. , vol.112 , pp. 149-158
    • Marks, P.W.1    Hendey, B.2    Maxfield, F.R.3
  • 65
    • 0026742310 scopus 로고
    • Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
    • Matsuyoshi, N., M. Hamaguchi, S. Taniguchi, A. Nagafuchi, S. Tsukita, and M. Takeichi. 1992. Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol. 118:703-714.
    • (1992) J. Cell Biol. , vol.118 , pp. 703-714
    • Matsuyoshi, N.1    Hamaguchi, M.2    Taniguchi, S.3    Nagafuchi, A.4    Tsukita, S.5    Takeichi, M.6
  • 66
    • 0027398589 scopus 로고
    • Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion
    • McNeill, H., T.A. Ryan, S.J. Smith, and W.J. Nelson. 1993. Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion. J. Cell Biol. 120:1217-1226.
    • (1993) J. Cell Biol. , vol.120 , pp. 1217-1226
    • McNeill, H.1    Ryan, T.A.2    Smith, S.J.3    Nelson, W.J.4
  • 67
    • 0023104271 scopus 로고
    • Multiple calcium channels and neuronal function
    • Miller, R.J. 1987. Multiple calcium channels and neuronal function. Science (Wash. DC). 235:46-52.
    • (1987) Science (Wash. DC) , vol.235 , pp. 46-52
    • Miller, R.J.1
  • 68
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S. Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science (Wash. DC). 267:883-885.
    • (1995) Science (Wash. DC) , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.2    Yamada, K.M.3
  • 70
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., H. Teramoto, J.S. Gutkind, and K.M. Yamada. 1996. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135:1633-1642.
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 71
    • 0029558225 scopus 로고
    • Control of N-cadherin-mediated intercellular adhesion in migrating neural crest cells in vitro
    • Monier-Gavelle, F., and J.-L. Duband. 1995. Control of N-cadherin-mediated intercellular adhesion in migrating neural crest cells in vitro. J. Cell Sci. 108:3839-3853.
    • (1995) J. Cell Sci. , vol.108 , pp. 3839-3853
    • Monier-Gavelle, F.1    Duband, J.-L.2
  • 72
    • 0023872138 scopus 로고
    • Transmembrane orientation of the fibronectin receptor complex (integrin) demonstrated directly by a combination of immunocytochemical approaches
    • Mueller, S.C., T. Hasegawa, S.S. Yamada, K.M. Yamada, and W.-T. Chen. 1988. Transmembrane orientation of the fibronectin receptor complex (integrin) demonstrated directly by a combination of immunocytochemical approaches. J. Histochem. Cytochem. 36:297-306.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 297-306
    • Mueller, S.C.1    Hasegawa, T.2    Yamada, S.S.3    Yamada, K.M.4    Chen, W.-T.5
  • 73
    • 0029065541 scopus 로고
    • Neural crest cell-cell adhesion controlled by sequential and subpopulation-specific expression of novel cadherins
    • Nakagawa, S., and M. Takeichi. 1995. Neural crest cell-cell adhesion controlled by sequential and subpopulation-specific expression of novel cadherins. Development (Camb.). 121:1321-1332.
    • (1995) Development (Camb.) , vol.121 , pp. 1321-1332
    • Nakagawa, S.1    Takeichi, M.2
  • 74
    • 0002760170 scopus 로고
    • The cadherin/catenin complex: Connections to multiple cellular processes involved in cell adhesion, proliferation and morphogenesis
    • Näthke, I.S., L. Hinck, and W.J. Nelson. 1995. The cadherin/catenin complex: connections to multiple cellular processes involved in cell adhesion, proliferation and morphogenesis. Semin. Dev. Biol. 6:89-95.
    • (1995) Semin. Dev. Biol. , vol.6 , pp. 89-95
    • Näthke, I.S.1    Hinck, L.2    Nelson, W.J.3
  • 75
    • 0022503377 scopus 로고
    • The migration of neural crest cells
    • Newgreen, D.F., and C.A. Erickson. 1986. The migration of neural crest cells. Int. Rev. Cytol. 103:89-145.
    • (1986) Int. Rev. Cytol. , vol.103 , pp. 89-145
    • Newgreen, D.F.1    Erickson, C.A.2
  • 76
    • 0029089336 scopus 로고
    • Control of epitheliomesenchymal transformation. I. Events in the onset of neural crest cell migration are separable and inducible by protein kinase inhibitors
    • Newgreen, D.F., and J. Minichiello. 1995. Control of epitheliomesenchymal transformation. I. Events in the onset of neural crest cell migration are separable and inducible by protein kinase inhibitors. Dev. Biol. 170: 91-101.
    • (1995) Dev. Biol. , vol.170 , pp. 91-101
    • Newgreen, D.F.1    Minichiello, J.2
  • 77
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and in tumor promotion
    • Nishizuka, Y. 1984. The role of protein kinase C in cell surface signal transduction and in tumor promotion. Nature (Lond.). 308:693-698.
    • (1984) Nature (Lond.) , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 78
    • 0025064957 scopus 로고
    • Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin
    • Ozawa, M., and R. Kemler. 1990. Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin. J. Cell Biol. 111:1645-1650.
    • (1990) J. Cell Biol. , vol.111 , pp. 1645-1650
    • Ozawa, M.1    Kemler, R.2
  • 79
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher, M.D., and E. Ruoslahti. 1987. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262:17294-17298.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 80
    • 0028987228 scopus 로고
    • Control of α5β1 integrin/fibronectin interaction in vitro by the serine/threonine protein phosphatase calcineurin
    • Pomiès, P., P. Frachet, and M.R. Block. 1995. Control of α5β1 integrin/fibronectin interaction in vitro by the serine/threonine protein phosphatase calcineurin. Biochemistry. 34:5104-5112.
    • (1995) Biochemistry , vol.34 , pp. 5104-5112
    • Pomiès, P.1    Frachet, P.2    Block, M.R.3
  • 81
    • 0017102422 scopus 로고
    • Biological applications of ionophores
    • Pressman, B.C. 1976. Biological applications of ionophores. Annu. Rev. Biochem. 45:501-529.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 501-529
    • Pressman, B.C.1
  • 82
    • 0025788512 scopus 로고
    • Functional evidence for three distinct and independently inhibitable adhesion activities mediated by the human integrin VLA-4. Correlation with distinct α4 epitopes
    • Pulido, R., M.J. Elices, M.R. Campanero, L. Osborn, S. Schiffer, A. Garcia-Pardo, R. Lobb, M.E. Hemler, and F. Sanchez-Madrid. 1991. Functional evidence for three distinct and independently inhibitable adhesion activities mediated by the human integrin VLA-4. Correlation with distinct α4 epitopes. J. Biol. Chem. 266:10241-10245.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10241-10245
    • Pulido, R.1    Elices, M.J.2    Campanero, M.R.3    Osborn, L.4    Schiffer, S.5    Garcia-Pardo, A.6    Lobb, R.7    Hemler, M.E.8    Sanchez-Madrid, F.9
  • 83
    • 0020581958 scopus 로고
    • Neural crest cell migration: Requirements for exogenous fibronectin and high cell density
    • Rovasio, R.A., A. Delouvée, K.M. Yamada, R. Timpl, and J.P. Thiery. 1983. Neural crest cell migration: requirements for exogenous fibronectin and high cell density. J. Cell Biol. 96:462-473.
    • (1983) J. Cell Biol. , vol.96 , pp. 462-473
    • Rovasio, R.A.1    Delouvée, A.2    Yamada, K.M.3    Timpl, R.4    Thiery, J.P.5
  • 84
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium
    • Schwartz, M.A. 1993. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium. J. Cell Biol. 120:1003-1010.
    • (1993) J. Cell Biol. , vol.120 , pp. 1003-1010
    • Schwartz, M.A.1
  • 85
    • 0028179351 scopus 로고
    • αv integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion
    • Schwartz, M.A., and K. Denninghoff. 1994. αv integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion. J. Biol. Chem. 269:11133-11137.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11133-11137
    • Schwartz, M.A.1    Denninghoff, K.2
  • 87
    • 0027170760 scopus 로고
    • A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells
    • Schwartz, M.A., E.J. Brown, and B. Fazeli. 1993. A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. J. Biol. Chem. 268:19931-19934.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19931-19934
    • Schwartz, M.A.1    Brown, E.J.2    Fazeli, B.3
  • 88
    • 84907115825 scopus 로고
    • Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells
    • Shibamoto, S., M. Hayakawa, H. Takeuchi, T. Hori, N. Oku, K. Miyazawa, N. Kitamura, M. Takeichi, and F. Ito. 1994. Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells. Cell Adh. Commun. 1:295-305.
    • (1994) Cell Adh. Commun. , vol.1 , pp. 295-305
    • Shibamoto, S.1    Hayakawa, M.2    Takeuchi, H.3    Hori, T.4    Oku, N.5    Miyazawa, K.6    Kitamura, N.7    Takeichi, M.8    Ito, F.9
  • 89
    • 0026784637 scopus 로고
    • Cadherin dysfunction in a human cancer cell line: Possible involvement of loss of α-catenin expression in reduced cell-cell adhesiveness
    • Shimoyama, Y., A. Nagafuchi, S. Fujita, M. Gotoh, M. Takeichi, S. Tsukita, and S. Hirohashi. 1992. Cadherin dysfunction in a human cancer cell line: possible involvement of loss of α-catenin expression in reduced cell-cell adhesiveness. Cancer Res. 52:5770-5774.
    • (1992) Cancer Res. , vol.52 , pp. 5770-5774
    • Shimoyama, Y.1    Nagafuchi, A.2    Fujita, S.3    Gotoh, M.4    Takeichi, M.5    Tsukita, S.6    Hirohashi, S.7
  • 90
    • 0025933683 scopus 로고
    • Biosynthesis of the cell adhesion molecule uvomorulin (E-cadherin) in Madin-Darby canine kidney epithelial cells
    • Shore, E.M., and W.J. Nelson. 1991. Biosynthesis of the cell adhesion molecule uvomorulin (E-cadherin) in Madin-Darby canine kidney epithelial cells. J. Biol. Chem. 266:19672-19680.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19672-19680
    • Shore, E.M.1    Nelson, W.J.2
  • 91
    • 0031025120 scopus 로고    scopus 로고
    • Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium
    • Sjaastad, M.D., and W.J. Nelson. 1997. Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium. Bioessays. 19:47-55.
    • (1997) Bioessays , vol.19 , pp. 47-55
    • Sjaastad, M.D.1    Nelson, W.J.2
  • 92
    • 0028176375 scopus 로고
    • Alterations in β-catenin phosphorylation and plakoglobin expression in human breast cancer cells
    • Sommers, C.L., E.P. Gelmann, R. Kemler, P. Cowin, and S.W. Byers. 1994. Alterations in β-catenin phosphorylation and plakoglobin expression in human breast cancer cells. Cancer Res. 54:3544-3552.
    • (1994) Cancer Res. , vol.54 , pp. 3544-3552
    • Sommers, C.L.1    Gelmann, E.P.2    Kemler, R.3    Cowin, P.4    Byers, S.W.5
  • 93
    • 0029615381 scopus 로고
    • V-src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and β-catenin is not required for the shift
    • Takeda, H., A. Nagafuchi, S. Yonemura, S. Tsukita, J. Behrens, W. Birchmeier, and S. Tsukita. 1995. V-src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and β-catenin is not required for the shift. J. Cell Biol. 131:1839-1847.
    • (1995) J. Cell Biol. , vol.131 , pp. 1839-1847
    • Takeda, H.1    Nagafuchi, A.2    Yonemura, S.3    Tsukita, S.4    Behrens, J.5    Birchmeier, W.6    Tsukita, S.7
  • 94
    • 0017758251 scopus 로고
    • Functional correlation between cell adhesive properties and some cell surface proteins
    • Takeichi, M. 1977. Functional correlation between cell adhesive properties and some cell surface proteins. J. Cell Biol. 75:464-474.
    • (1977) J. Cell Biol. , vol.75 , pp. 464-474
    • Takeichi, M.1
  • 95
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • Takeichi, M. 1993. Cadherins in cancer: implications for invasion and metastasis. Curr. Opin. Cell Biol. 5:806-811.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 806-811
    • Takeichi, M.1
  • 96
    • 0029160437 scopus 로고
    • Morphogenetic roles of cadherins
    • Takeichi, M. 1995. Morphogenetic roles of cadherins. Curr. Opin. Cell Biol. 7:619-627.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 99
    • 0020456137 scopus 로고
    • Pathways and mechanism of avian trunk neural crest cell migration and localization
    • Thiery, J.P., J.-L. Duband, and A. Delouvée. 1982. Pathways and mechanism of avian trunk neural crest cell migration and localization. Dev. Biol. 93:324-343.
    • (1982) Dev. Biol. , vol.93 , pp. 324-343
    • Thiery, J.P.1    Duband, J.-L.2    Delouvée, A.3
  • 100
    • 33845560024 scopus 로고
    • Structure of ionomycin, a novel diacidic polyether antibiotic having high affinity for calcium ions
    • Toeplitz, B.K., A.I. Cohen, P.T. Funke, W.L. Parker, and J.Z. Gougoutas. 1979. Structure of ionomycin, a novel diacidic polyether antibiotic having high affinity for calcium ions. J. Am. Chem. Soc. 101:3344-3446.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3344-3446
    • Toeplitz, B.K.1    Cohen, A.I.2    Funke, P.T.3    Parker, W.L.4    Gougoutas, J.Z.5
  • 102
    • 0025947138 scopus 로고
    • Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases
    • Uehara, V., and H. Fukazawa. 1991. Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases. Methods Enzymol. 201:370-379.
    • (1991) Methods Enzymol. , vol.201 , pp. 370-379
    • Uehara, V.1    Fukazawa, H.2
  • 104
    • 45149137825 scopus 로고
    • Inhibition of epidermal growth factor-induced DNA synthesis by tyrosine kinase inhibitors
    • Umezawa, K., T. Hori, H. Tajima, M. Imoto, K. Isshiki, and T. Takeuchi. 1990. Inhibition of epidermal growth factor-induced DNA synthesis by tyrosine kinase inhibitors. FEBS Lett. 260:198-200.
    • (1990) FEBS Lett. , vol.260 , pp. 198-200
    • Umezawa, K.1    Hori, T.2    Tajima, H.3    Imoto, M.4    Isshiki, K.5    Takeuchi, T.6
  • 106
    • 0025818032 scopus 로고
    • Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role
    • Vleminckx, K., L. Vakaet, M. Mareel, W. Fiers, and F. Van Roy. 1991. Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell. 66:107-119.
    • (1991) Cell , vol.66 , pp. 107-119
    • Vleminckx, K.1    Vakaet, L.2    Mareel, M.3    Fiers, W.4    Van Roy, F.5
  • 108
    • 0026114963 scopus 로고
    • Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells
    • Volberg, T., B. Geiger, R. Dror, and Y. Zick. 1991. Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells. Cell Regul. 2: 105-120.
    • (1991) Cell Regul. , vol.2 , pp. 105-120
    • Volberg, T.1    Geiger, B.2    Dror, R.3    Zick, Y.4
  • 110
    • 0025369365 scopus 로고
    • Cleavage of A-CAM by endogenous proteinases in cultured lens cells and in developing chick embryos
    • Volk, T., T. Volberg, I. Sabanay, and B. Geiger. 1990. Cleavage of A-CAM by endogenous proteinases in cultured lens cells and in developing chick embryos. Dev. Biol. 139:314-326.
    • (1990) Dev. Biol. , vol.139 , pp. 314-326
    • Volk, T.1    Volberg, T.2    Sabanay, I.3    Geiger, B.4
  • 111
    • 0024110741 scopus 로고
    • The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: Preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa
    • Wayner, E.A., W.G. Carter, R.S. Piotrowicz, and T.J. Kunicki. 1988. The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa. J. Cell Biol. 107: 1881-1891.
    • (1988) J. Cell Biol. , vol.107 , pp. 1881-1891
    • Wayner, E.A.1    Carter, W.G.2    Piotrowicz, R.S.3    Kunicki, T.J.4
  • 112
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada, K.M., and S. Miyamoto. 1995. Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7:681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2


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